Abstract:
:The fibronectin type II (FnII) domain, present in diverse vertebrate proteins, plays crucial roles in several fundamental biological processes. PDC-109, the major bovine seminal plasma protein, contains two FnII domains that bind to choline phospholipids on sperm plasma membrane and induce lipid efflux crucial for successful fertilization. PDC-109 also exhibits chaperone-like activity and protects other proteins against various types of stress. Here, we show that a core tryptophan residue is highly conserved across species in the FnII domains. Mutation of conserved tryptophan residues W47, W93, and W106 in the FnII domains of PDC-109 to alanine leads to drastic decrease or complete abolition of membrane-binding and chaperone-like activities. These observations suggest that conserved tryptophans are important for the function of FnII proteins.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Singh BP,Asthana A,Basu A,Tangirala R,Mohan Rao C,Swamy MJdoi
10.1002/1873-3468.13617subject
Has Abstractpub_date
2020-02-01 00:00:00pages
509-518issue
3eissn
0014-5793issn
1873-3468journal_volume
594pub_type
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